Isolation and structure elucidation of a novel 5-kDa peptide from neurohaemal lobes of the corpora cardiaca of Locusta migratoria (Insecta, Orthoptera).
Two predominant peptides have been isolated from neurohaemal lobes of corpora cardiaca of 8000 adults of Locusta migratoria. Both peptides have been unambiguously characterized by automated peptide microsequencing and liquid secondary-ion mass spectrometry as a 50-residue peptide (5K peptide) and a 48-residue isologue (5K' peptide). Computer search of sequence data banks did not reveal any significant similarity with other identified proteins. The 5K peptides are remarkably rich in alanine residues (25%) and contain a stretch of five consecutive alanines. This structure suggests that these molecules could correspond to spacer peptides. This assumption is corroborated in the accompanying paper [Lagueux et al. (1990) Eur. J. Biochem. 187, 249-254] on the molecular cloning of the precursor protein which attributes to the 5K peptides a role analogous to that of the C peptides of insulins.
Hietter
H
H
Laboratoire de Chimie Organiques des Substances Naturelles, associé au Centre National de la Recherche Scientifique, Strasbourg, France.
Van Dorsselaer
A
A
Green
B
B
Denoroy
L
L
Hoffmann
J
J
Luu
B
B
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006110:Grasshoppers / Q000032:analysis*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009479:Neuropeptides / Q000302:isolation & purification*; D009490:Neurosecretory Systems / Q000032:analysis*; D010446:Peptide Fragments / Q000302:isolation & purification
D000596:Amino Acids; D009479:Neuropeptides; D010446:Peptide Fragments